A three (3) year project on laser Raman spectroscopy of biopolymers is in progress. It has been demonstrated that Raman spectroscopy is sensitive to insulin conformation. Striking and interesting spectral changes upon globular-fibrous transformation of insulin have been analyzed in detail. We have established that the fibrous insulin is predominantly beta structure both in the solid state and in aqueous environment. This is in contrary to the earlier concept, in which the fibrils were thought to be arrays of only slightly distorted globular insulin molecules. It is also established that Raman and infrared techniques do not detect the same amide I vibrational modes in proteins as well as in peptide homopolymers. At present, we are studying the time-dependent Raman spectra of acidic aqueous glucagon and the spectra of papain and carboxypeptidases.